This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
1ebu
From Proteopedia
| Line 4: | Line 4: | ||
|PDB= 1ebu |SIZE=350|CAPTION= <scene name='initialview01'>1ebu</scene>, resolution 2.60Å | |PDB= 1ebu |SIZE=350|CAPTION= <scene name='initialview01'>1ebu</scene>, resolution 2.60Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=NDA:3-AMINOMETHYL-PYRIDINIUM-ADENINE-DINUCLEOTIDE'>NDA</scene> | + | |LIGAND= <scene name='pdbligand=HSE:L-HOMOSERINE'>HSE</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=NDA:3-AMINOMETHYL-PYRIDINIUM-ADENINE-DINUCLEOTIDE'>NDA</scene> |
| - | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Homoserine_dehydrogenase Homoserine dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.3 1.1.1.3] </span> | |
|GENE= HOM6P ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae]) | |GENE= HOM6P ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1ebf|1EBF]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ebu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ebu OCA], [http://www.ebi.ac.uk/pdbsum/1ebu PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ebu RCSB]</span> | ||
}} | }} | ||
| Line 27: | Line 30: | ||
[[Category: Thompson, P R.]] | [[Category: Thompson, P R.]] | ||
[[Category: Wright, G D.]] | [[Category: Wright, G D.]] | ||
| - | [[Category: HSE]] | ||
| - | [[Category: NA]] | ||
| - | [[Category: NDA]] | ||
[[Category: analogue]] | [[Category: analogue]] | ||
[[Category: dehydrogenase]] | [[Category: dehydrogenase]] | ||
| Line 36: | Line 36: | ||
[[Category: ternary]] | [[Category: ternary]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:59:25 2008'' |
Revision as of 16:59, 30 March 2008
| |||||||
| , resolution 2.60Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , | ||||||
| Gene: | HOM6P (Saccharomyces cerevisiae) | ||||||
| Activity: | Homoserine dehydrogenase, with EC number 1.1.1.3 | ||||||
| Related: | 1EBF
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
HOMOSERINE DEHYDROGENASE COMPLEX WITH NAD ANALOGUE AND L-HOMOSERINE
Overview
The structure of the antifungal drug target homoserine dehydrogenase (HSD) was determined from Saccharomyces cerevisiae in apo and holo forms, and as a ternary complex with bound products, by X-ray diffraction. The three forms show that the enzyme is a dimer, with each monomer composed of three regions, the nucleotide-binding region, the dimerization region and the catalytic region. The dimerization and catalytic regions have novel folds, whereas the fold of the nucleotide-binding region is a variation on the Rossmann fold. The novel folds impose a novel composition and arrangement of active site residues when compared to all other currently known oxidoreductases. This observation, in conjunction with site-directed mutagenesis of active site residues and steady-state kinetic measurements, suggest that HSD exhibits a new variation on dehydrogenase chemistry.
About this Structure
1EBU is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.
Reference
Crystal structures of homoserine dehydrogenase suggest a novel catalytic mechanism for oxidoreductases., DeLaBarre B, Thompson PR, Wright GD, Berghuis AM, Nat Struct Biol. 2000 Mar;7(3):238-44. PMID:10700284
Page seeded by OCA on Sun Mar 30 19:59:25 2008
